RPV1_VITRO
ID RPV1_VITRO Reviewed; 1398 AA.
AC V9M2S5;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Disease resistance protein RPV1 {ECO:0000305};
DE AltName: Full=NAD(+) hydrolase RPV1;
DE EC=3.2.2.6 {ECO:0000305|PubMed:31439792};
DE AltName: Full=Resistance to Plasmopara viticola protein {ECO:0000303|PubMed:24033846};
DE Short=MrRVP1 {ECO:0000303|PubMed:24033846};
GN Name=RPV1 {ECO:0000303|PubMed:24033846};
OS Vitis rotundifolia (Muscadine grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=103349;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 1370-LYS-ARG-1371.
RX PubMed=24033846; DOI=10.1111/tpj.12327;
RA Feechan A., Anderson C., Torregrosa L., Jermakow A., Mestre P.,
RA Wiedemann-Merdinoglu S., Merdinoglu D., Walker A.R., Cadle-Davidson L.,
RA Reisch B., Aubourg S., Bentahar N., Shrestha B., Bouquet A.,
RA Adam-Blondon A.F., Thomas M.R., Dry I.B.;
RT "Genetic dissection of a TIR-NB-LRR locus from the wild North American
RT grapevine species Muscadinia rotundifolia identifies paralogous genes
RT conferring resistance to major fungal and oomycete pathogens in cultivated
RT grapevine.";
RL Plant J. 76:661-674(2013).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
RN [3] {ECO:0007744|PDB:5KU7}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-193, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF ARG-36; ASP-41; HIS-42; PRO-121; ARG-125 AND GLY-161.
RX PubMed=28008335; DOI=10.3389/fpls.2016.01850;
RA Williams S.J., Yin L., Foley G., Casey L.W., Outram M.A., Ericsson D.J.,
RA Lu J., Boden M., Dry I.B., Kobe B.;
RT "Structure and Function of the TIR Domain from the Grape NLR Protein
RT RPV1.";
RL Front. Plant Sci. 7:1850-1850(2016).
CC -!- FUNCTION: Disease resistance (R) protein that confers resistance to
CC multiple powdery and downy mildew by promoting cell death
CC (PubMed:24033846, PubMed:28008335). Acts as a NAD(+) hydrolase
CC (NADase): in response to activation, catalyzes cleavage of NAD(+) into
CC ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a
CC defense system that promotes cell death (PubMed:31439792).
CC {ECO:0000269|PubMed:24033846, ECO:0000269|PubMed:28008335,
CC ECO:0000269|PubMed:31439792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000305|PubMed:31439792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000305|PubMed:31439792};
CC -!- SUBUNIT: Homodimer; homodimerization is required for NAD(+) hydrolase
CC (NADase) activity. {ECO:0000305|PubMed:28008335}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24033846}. Cytoplasm
CC {ECO:0000269|PubMed:24033846}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
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DR EMBL; JQ904634; AGC24028.1; -; Genomic_DNA.
DR PDB; 5KU7; X-ray; 2.30 A; A/B=20-193.
DR PDBsum; 5KU7; -.
DR AlphaFoldDB; V9M2S5; -.
DR SMR; V9M2S5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 8.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Leucine-rich repeat; NAD; Nucleus;
KW Plant defense; Repeat.
FT CHAIN 1..1398
FT /note="Disease resistance protein RPV1"
FT /id="PRO_0000448794"
FT DOMAIN 22..185
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 201..440
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 203..225
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 423..447
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 478..504
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 535..560
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 610..632
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 633..657
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 678..702
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 703..726
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 728..750
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 751..773
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 775..797
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 798..820
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 822..844
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 845..867
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 869..891
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 892..914
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 916..938
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 939..961
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 963..985
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 986..1008
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 1010..1032
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 1033..1055
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 1079..1102
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 1105..1128
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 1346..1369
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REGION 1315..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1369..1373
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24033846"
FT COMPBIAS 1315..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 31..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT BINDING 63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT MUTAGEN 36
FT /note="R->A: Abolished ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 41
FT /note="D->A: Abolished ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 42
FT /note="H->A: Abolished ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 121
FT /note="P->Y: Decreased ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 125
FT /note="R->A: Decreased ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 161
FT /note="G->R: Decreased ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28008335"
FT MUTAGEN 1370..1371
FT /note="KR->TS: Abolished nuclear localization."
FT /evidence="ECO:0000269|PubMed:24033846"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:5KU7"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:5KU7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:5KU7"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:5KU7"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:5KU7"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5KU7"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5KU7"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5KU7"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5KU7"
FT HELIX 170..191
FT /evidence="ECO:0007829|PDB:5KU7"
SQ SEQUENCE 1398 AA; 158727 MW; 37B810662F9E2295 CRC64;
MASTSSFRAS SSSSTPSIPR TTTYDVFLSF RGEDTRYNFT DHLYSALGRR GIRTFRDDRL
RRGEAIAPEL LKAIEESRSS VIVFSENYAH SRWCLDELVK IMECQKDLGH AVFPIFYHVD
PSHVRKQEGS FGEAFAGYEE NWKDKIPRWR TALTEAANLS GWHLLDDRYE SNQIKEITNS
IFRQLKCKRL DVGANLVGID SHVKEMILRL HLESSDVRMV GIYGVGGIGK TTIAKVIYNE
LSCEFEYMSF LENIREGSNP QVLFHLQNQL LGDILEGEGS QNISSVAHRA SMIKDILLSR
RVFIVLDDVD DLSQLEYLLG HREWLGEGSR VIITTRNKHV LAVQEVDDLY EVEGLNFEEA
CELFSLYAFK QNLPKSDYRN LTCRVVGYCQ GLPLALKVLG SLLCKKTIPQ WEGELKKLDS
EPKADIHKVL KRSYDGLDRI DKNIFLDLAC FFKGEGRDFV LRILDGCDFP AETGISNLND
LCLITLPYNQ ICMHDLIQQM GWEIVRENFP VEPNKWSRLW DPCDFERALT ADEGIKSVET
MSLDLSKLKR VCSNSNVFAK MTKLRLLKVY SSSDIDSAHG DSDEDIEEVY DVVMKDASKM
QLGQSFKFPS YELRYLRWDG YPLDSLPLNF DGGKLVELHL KCSNIKQLWQ GHKDLERLKV
IDLSYSRKLS QMSEFSSMPN LERLCLSGCV SLIDIHPSVG NMKKLTTLSL RSCNKLKNLP
DSIGDLESLE SLYLSNCSKF EKFPEKGGNM KSLTELDLKN TAIKDLPDSI GDLESLESLY
LSNCSKFEKF PEKGGNMKSL TELDLKNTAI KDLPDSIGDL ESLEILNLSD CAKFEKFPEK
GGNMKSLKEL DLQNTAIKDL PDSIGDLKSL KYLSLSDCSK FEKFPEKGGN MKRLLQLILS
NTAIKDLPDS IGDLESLKYL YLSDCSKFEK FPEKGGNMKS LTELDLKNTA IKDLPDSIGD
LESLEILNLS DCAKFEKFPE KGGNMKSLKE LDLQNTAIKD LPDSIGDLES LKYLYLSDCS
KFEKFPEKGG NMKSLLQLIL SNTAIKDLPD SIGDLESLEY LHLSVCSKFE KFPEKGGNMK
SLRELGLRNT AIKDLPDSIG DLESLEMLSL SNCPKFEVLP LSLKAIDAHL CTSKEDLSRL
LWLCHRNWLK STTEEFDRWQ LSAFIPESSG IPEWITYQNL GSEVTEKLPI NWCEDPDFPG
FVLSCVYRPS CDYSSAYIFC HDFKCELNLH GNGFRFRDVC YHECWCDCHV NFKDSRDLVC
VYWYPKTAIP EEDHHKYTHI NASFKSDEVK IKKCGINVIF LGDQRNHMPM LEHPQNSGDN
GSALQDANGN VHGANQDDEH YHIPLLDLLR NLSLGDNGSV VLEDTLGNRK RRRNDSLPDV
VEEPLYKRLG GPHTEISL
